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Related Experiment Videos

The binding site on human immunoglobulin E for its high affinity receptor

L Presta1, R Shields, L O'Connell

  • 1Department of Protein Engineering, Genentech Inc., South San Francisco, California 94080.

The Journal of Biological Chemistry
|October 21, 1994
PubMed
Summary

Researchers identified key amino acids in Immunoglobulin (Ig) E that bind to the Fc epsilon RI receptor. These findings reveal electrostatic interactions and suggest potential for engineering IgG to bind Fc epsilon RI.

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Area of Science:

  • Immunology
  • Structural Biology
  • Allergy Research

Background:

  • Immunoglobulin (Ig) E antibodies trigger allergic reactions by binding to high-affinity Fc epsilon RI receptors on mast cells and basophils.
  • The primary binding site for Fc epsilon RI on IgE is located within its third constant domain (Fc epsilon 3).

Purpose of the Study:

  • To pinpoint the specific amino acids in human IgE responsible for binding to the human Fc epsilon RI receptor.
  • To elucidate the structural basis and interaction forces governing IgE-Fc epsilon RI binding.

Main Methods:

  • Utilized homology scanning mutagenesis and site-directed mutagenesis on a model of the IgE Fc epsilon 3 domain.
  • Replaced individual amino acid residues to assess their impact on Fc epsilon RI binding.

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Main Results:

  • Identified a critical binding site on the Fc epsilon 3 domain, comprising three loops containing specific residues (Arg-408, Ser-411, Lys-415, Glu-452, Arg-465, Met-469).
  • Observed a high proportion of charged residues, indicating that electrostatic interactions are crucial for IgE-Fc epsilon RI binding.
  • Demonstrated that introducing these IgE loops into the IgG C gamma 2 domain can confer Fc epsilon RI binding capability to IgG.

Conclusions:

  • The identified amino acid residues and loops form a distinct ridge essential for IgE-Fc epsilon RI interaction.
  • Electrostatic forces play a dominant role in the binding of IgE to its high-affinity receptor.
  • The study provides a foundation for potential therapeutic strategies by enabling the engineering of Fc epsilon RI binding into other antibody classes.